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Volumn 78, Issue 22, 2004, Pages 12428-12437

Emergence of a drug-dependent human immunodeficiency virus type 1 variant during therapy with the T20 fusion inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

ENFUVIRTIDE; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; PROTEINASE INHIBITOR; RNA DIRECTED DNA POLYMERASE; VIRUS ENVELOPE PROTEIN;

EID: 7644236011     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.22.12428-12437.2004     Document Type: Article
Times cited : (130)

References (45)
  • 1
    • 0042924167 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry with fusion inhibitors
    • Baldwin, C. E., R. W. Sanders, and B. Berkhout. 2003. Inhibiting HIV-1 entry with fusion inhibitors. Curr. Med. Chem. 10:1633-1642.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1633-1642
    • Baldwin, C.E.1    Sanders, R.W.2    Berkhout, B.3
  • 2
    • 0035815637 scopus 로고    scopus 로고
    • HIV-1 RNA editing, hypermutation and error-prone reverse transcription
    • Berkhout, B., A. T. Das, and N. Beerens. 2001. HIV-1 RNA editing, hypermutation and error-prone reverse transcription. Science 292:7.
    • (2001) Science , vol.292 , pp. 7
    • Berkhout, B.1    Das, A.T.2    Beerens, N.3
  • 4
    • 7644220399 scopus 로고
    • W. H. Freeman and Company, New York, N.Y.
    • Cantor, C., and P. Schimmel. 1980. Biophysical chemistry, part III. W. H. Freeman and Company, New York, N.Y.
    • (1980) Biophysical Chemistry , Issue.3 PART
    • Cantor, C.1    Schimmel, P.2
  • 5
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., D. Fass, J. M. Berger, and P. S. Kim. 1997. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89:263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 6
    • 0028107566 scopus 로고
    • Functional role of the zipper motif region of human immunodeficiency virus type 1 transmembrane protein gp41
    • Chen, S. S. 1994. Functional role of the zipper motif region of human immunodeficiency virus type 1 transmembrane protein gp41. J. Virol. 68:2002-2010.
    • (1994) J. Virol. , vol.68 , pp. 2002-2010
    • Chen, S.S.1
  • 7
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Chen, Y. H., J. T. Yang, and K. H. Chau. 1974. Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry 13:3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 8
    • 0028229079 scopus 로고
    • Deletion of a single N-linked glycosylation site from the transmembrane envelope protein of human immunodeficiency virus type 1 stops cleavage and transport of gp160 preventing env-mediated fusion
    • Dash, B., A. McIntosh, W. Barrett, and R. Daniels. 1994. Deletion of a single N-linked glycosylation site from the transmembrane envelope protein of human immunodeficiency virus type 1 stops cleavage and transport of gp160 preventing env-mediated fusion. J. Gen. Virol. 75:1389-1397.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1389-1397
    • Dash, B.1    McIntosh, A.2    Barrett, W.3    Daniels, R.4
  • 9
    • 0026533141 scopus 로고
    • Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function
    • Dedera, D. A., R. L. Gu, and L. Ratner. 1992. Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function. Virology 187:377-382.
    • (1992) Virology , vol.187 , pp. 377-382
    • Dedera, D.A.1    Gu, R.L.2    Ratner, L.3
  • 10
    • 0035862545 scopus 로고    scopus 로고
    • N- and C-domains of HIV-1 gp41: Mutation, structure and functions
    • Dong, X. N., Y. Xiao, M. P. Dierich, and Y. H. Chen. 2001. N- and C-domains of HIV-1 gp41: mutation, structure and functions. Immunol. Lett. 75:215-220.
    • (2001) Immunol. Lett. , vol.75 , pp. 215-220
    • Dong, X.N.1    Xiao, Y.2    Dierich, M.P.3    Chen, Y.H.4
  • 11
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M., and P. S. Kim. 2001. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70:777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 12
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. 1967. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6:1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 13
    • 0037119035 scopus 로고    scopus 로고
    • Resistance mutation in HIV entry inhibitors
    • Hanna, S. L., C. Yang, S. M. Owen, and R. B. Lal. 2002. Resistance mutation in HIV entry inhibitors. AIDS 16:1603-1608.
    • (2002) AIDS , vol.16 , pp. 1603-1608
    • Hanna, S.L.1    Yang, C.2    Owen, S.M.3    Lal, R.B.4
  • 14
    • 0035937255 scopus 로고    scopus 로고
    • Thermodynamics of trimer-of-hairpins formation by the SIV gp41 envelope protein
    • Jelesarov, I., and M. Lu. 2001. Thermodynamics of trimer-of-hairpins formation by the SIV gp41 envelope protein. J. Mol. Biol. 307:637-656.
    • (2001) J. Mol. Biol. , vol.307 , pp. 637-656
    • Jelesarov, I.1    Lu, M.2
  • 15
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson, M. L., J. J. Correia, D. A. Yphantis, and H. R. Halvorson. 1981. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys. J. 36:575-588.
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 16
    • 0035163480 scopus 로고    scopus 로고
    • Conserved, N-linked carbohydrates of human immunodeficiency virus type 1 gp41 are largely dispensable for viral replication
    • Johnson, W. E., J. M. Sauvron, and R. C. Desrosiers. 2001. Conserved, N-linked carbohydrates of human immunodeficiency virus type 1 gp41 are largely dispensable for viral replication. J. Virol. 75:11426-11436.
    • (2001) J. Virol. , vol.75 , pp. 11426-11436
    • Johnson, W.E.1    Sauvron, J.M.2    Desrosiers, R.C.3
  • 17
    • 0030896362 scopus 로고    scopus 로고
    • Initial appearance of the 184Ile variant in lamivudine-treated patients is caused by the mutational bias of the human immunodeficiency virus type 1 reverse transcriptase
    • Keulen, W., N. K. T. Back, A. van Wijk, C. A. B. Boucher, and B. Berkhout. 1997. Initial appearance of the 184Ile variant in lamivudine-treated patients is caused by the mutational bias of the human immunodeficiency virus type 1 reverse transcriptase. J. Virol. 71:3346-3350.
    • (1997) J. Virol. , vol.71 , pp. 3346-3350
    • Keulen, W.1    Back, N.K.T.2    Van Wijk, A.3    Boucher, C.A.B.4    Berkhout, B.5
  • 18
    • 0029885139 scopus 로고    scopus 로고
    • Nucleotide substitution patterns can predict the requirements for drug resistance of HIV-1 proteins
    • Keulen, W., C. Boucher, and B. Berkhout. 1996. Nucleotide substitution patterns can predict the requirements for drug resistance of HIV-1 proteins. Antiviral Res. 31:45-57.
    • (1996) Antiviral Res. , vol.31 , pp. 45-57
    • Keulen, W.1    Boucher, C.2    Berkhout, B.3
  • 20
    • 0038467539 scopus 로고    scopus 로고
    • Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope
    • Kilgore, N. R., K. Salzwedel, M. Reddick, G. P. Allaway, and C. T. Wild. 2003. Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope. J. Virol. 77:7669-7672.
    • (2003) J. Virol. , vol.77 , pp. 7669-7672
    • Kilgore, N.R.1    Salzwedel, K.2    Reddick, M.3    Allaway, G.P.4    Wild, C.T.5
  • 21
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82:488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 22
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • S. E. Harding, A. J. Rowe, and J. C. Horton (ed.), Royal Society of Chemistry, Cambridge, England
    • Laue, T. M., B. D. Shah, T. M. Ridgeway, and S. L. Pelletier. 1992. Computer-aided interpretation of analytical sedimentation data for proteins, p. 90-125. In S. E. Harding, A. J. Rowe, and J. C. Horton (ed.), Analytical ultracentrifugation in biochemistry and polymer science. Royal Society of Chemistry, Cambridge, England.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 24
    • 0026579886 scopus 로고
    • Mutational analysis of conserved N-linked glycosylation sites of human immunodeficiency virus type 1 gp41
    • Lee, W. R., X. F. Yu, W. J. Syu, M. Essex, and T. H. Lee. 1992. Mutational analysis of conserved N-linked glycosylation sites of human immunodeficiency virus type 1 gp41. J. Virol. 66:1799-1803.
    • (1992) J. Virol. , vol.66 , pp. 1799-1803
    • Lee, W.R.1    Yu, X.F.2    Syu, W.J.3    Essex, M.4    Lee, T.H.5
  • 26
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., S. C. Blacklow, and P. S. Kim. 1995. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2:1075-1082.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 27
    • 0035932984 scopus 로고    scopus 로고
    • In vitro evolution of a highly replicating, doxycycline-dependent HIV for applications in vaccine studies
    • Marzio, G., K. Verhoef, M. Vink, and B. Berkhout. 2001. In vitro evolution of a highly replicating, doxycycline-dependent HIV for applications in vaccine studies. Proc. Natl. Acad. Sci. USA 98:6342-6347.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6342-6347
    • Marzio, G.1    Verhoef, K.2    Vink, M.3    Berkhout, B.4
  • 28
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan, G. B., R. M. Markosyan, H. Hemmati, M. K. Delmedico, D. M. Lambert, and F. S. Cohen. 2000. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J. Cell Biol. 151:413-423.
    • (2000) J. Cell Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 29
    • 0141814730 scopus 로고    scopus 로고
    • The entry of entry inhibitors: A fusion of science and medicine
    • Moore, J. P., and R. W. Doms. 2003. The entry of entry inhibitors: A fusion of science and medicine. Proc. Natl. Acad. Sci. USA 100:10598-10606.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10598-10606
    • Moore, J.P.1    Doms, R.W.2
  • 30
    • 0034304841 scopus 로고    scopus 로고
    • New targets for inhibitors of HIV-1 replication
    • Moore, J. P., and M. Stevenson. 2000. New targets for inhibitors of HIV-1 replication. Nat. Rev. Mol. Cell. Biol. 1:40-49.
    • (2000) Nat. Rev. Mol. Cell. Biol. , vol.1 , pp. 40-49
    • Moore, J.P.1    Stevenson, M.2
  • 32
    • 0032520597 scopus 로고    scopus 로고
    • Role of gp41 glycosylation sites in the biological activity of human immunodeficiency virus type 1 envelope glycoprotein
    • Perrin, C., E. Fenouillet, and I. M. Jones. 1998. Role of gp41 glycosylation sites in the biological activity of human immunodeficiency virus type 1 envelope glycoprotein. Virology 242:338-345.
    • (1998) Virology , vol.242 , pp. 338-345
    • Perrin, C.1    Fenouillet, E.2    Jones, I.M.3
  • 33
    • 0037183892 scopus 로고    scopus 로고
    • Evolution of the gp41 env region in HIV-infected patients receiving T-20, a fusion inhibitor
    • Poveda, E., B. Rodes, C. Tore, L. Martin-Carhonero, J. Gonzalez-Lahoz, and V. Soriano. 2002. Evolution of the gp41 env region in HIV-infected patients receiving T-20, a fusion inhibitor. AIDS 16:1959-1961.
    • (2002) AIDS , vol.16 , pp. 1959-1961
    • Poveda, E.1    Rodes, B.2    Tore, C.3    Martin-Carhonero, L.4    Gonzalez-Lahoz, J.5    Soriano, V.6
  • 34
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency viras type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky, L. T., D. C. Shugars, and T. J. Matthews. 1998. Determinants of human immunodeficiency viras type 1 resistance to gp41-derived inhibitory peptides. J. Virol. 72:986-993.
    • (1998) J. Virol. , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 36
    • 3843108323 scopus 로고    scopus 로고
    • Mutational analyses and natural variability of the gp41 ectodomain
    • C. Kuiken, B. Foley, E. Freed, B. Hahn, P. Marx, F. McCutchan, J. Mellors, S. Wolinsky, and B. Korber (ed.), Los Alamos National Laboratory Theoretical Biology and Biophysics Group, Los Alamos, N.Mex.
    • Sanders, R. W., B. Korber, M. Lu, B. Berkhout, and J. P. Moore. 2002. Mutational analyses and natural variability of the gp41 ectodomain, p. 43-68. In C. Kuiken, B. Foley, E. Freed, B. Hahn, P. Marx, F. McCutchan, J. Mellors, S. Wolinsky, and B. Korber (ed.), HIV sequence compendium 2002. Los Alamos National Laboratory Theoretical Biology and Biophysics Group, Los Alamos, N.Mex.
    • (2002) HIV Sequence Compendium 2002 , pp. 43-68
    • Sanders, R.W.1    Korber, B.2    Lu, M.3    Berkhout, B.4    Moore, J.P.5
  • 38
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan, K., J. Liu, J. Wang, S. Shen, and M. Lu. 1997. Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. USA 94:12303-12308.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3    Shen, S.4    Lu, M.5
  • 39
    • 0035163747 scopus 로고    scopus 로고
    • Strict control of human immunodeficiency virus type 1 replication by a genetic switch: Tet for Tat
    • Verhoef, K., G. Marzio, W. Hillen, H. Bujard, and B. Berkhout. 2001. Strict control of human immunodeficiency virus type 1 replication by a genetic switch: Tet for Tat. J. Virol. 75:979-987.
    • (2001) J. Virol. , vol.75 , pp. 979-987
    • Verhoef, K.1    Marzio, G.2    Hillen, W.3    Bujard, H.4    Berkhout, B.5
  • 42
    • 0028575843 scopus 로고
    • Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex
    • Wild, C., J. W. Dubay, T. Greenwell, T. Baird, Jr., T. G. Oas, C. McDanal, E. Hunter, and T. Matthews. 1994. Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex. Proc. Natl. Acad. Sci. USA 91:12676-12680.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12676-12680
    • Wild, C.1    Dubay, J.W.2    Greenwell, T.3    Baird Jr., T.4    Oas, T.G.5    McDanal, C.6    Hunter, E.7    Matthews, T.8
  • 43
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild, C. T., D. C. Shugars, T. K. Greenwell, C. B. McDanal, and T. J. Matthews. 1994. Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. USA 91:9770-9774.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 44
    • 0037119027 scopus 로고    scopus 로고
    • Minimal variation in T-20 binding domain of different HIV-1 subtypes from antiretroviral-naive and -experienced patients
    • Xu, L., S. Hue, S. Taylor, D. Ratcliffe, J. A. Workman, S. Jackson, P. A. Cane, and D. Pillay. 2002. Minimal variation in T-20 binding domain of different HIV-1 subtypes from antiretroviral-naive and -experienced patients. AIDS 16:1684-1686.
    • (2002) AIDS , vol.16 , pp. 1684-1686
    • Xu, L.1    Hue, S.2    Taylor, S.3    Ratcliffe, D.4    Workman, J.A.5    Jackson, S.6    Cane, P.A.7    Pillay, D.8
  • 45
    • 0035805185 scopus 로고    scopus 로고
    • Primary genotypic resistance of HIV-1 to the fusion inhibitor T-20 in long-term infected patients
    • Zollner, B., H. H. Feucht, M. Schroter, P. Schafer, A. Plettenberg, A. Stoehr, and R. Laufs. 2001. Primary genotypic resistance of HIV-1 to the fusion inhibitor T-20 in long-term infected patients. AIDS 15:935-936.
    • (2001) AIDS , vol.15 , pp. 935-936
    • Zollner, B.1    Feucht, H.H.2    Schroter, M.3    Schafer, P.4    Plettenberg, A.5    Stoehr, A.6    Laufs, R.7


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